According to the American Cancer Society, in 2009 there were over 190,000 cases of prostate cancer reported and over 27,000 related deaths in the United States.
The ubiquitin-specific protease 2a (USP2a) can deubiquitinate the antiapoptotic proteins fatty acid synthase (FAS) and Mdm2. It has been shown that when USP2a is also overexpressed in nontransformed cells, it exhibits oncogenic behavior both in vitro and in vivo and also prevents apoptosis induced by chemotherapeutic agents. Notably, USP2a silencing in several human cancer cell lines can result in apoptosis.
USP2a is overexpressed in about 50% of human prostate tumors, and its oncogenicity in prostate cancer as well as its anti-apoptotic role in a variety of human tumor cell lines have been thoroughly demonstrated, making USP2a a good therapeutic target and prognostic marker in human cancer. However, currently available anti-USP2a antibodies are not specific enough and therefore are likely to cross-react with other proteins. This lack of specificity renders the current anti-USP2a antibodies less useful in both therapeutic discovery and as a marker in the analysis of patient tumors. Consequently, there remains a need for better USP2a antibodies useful in the diagnosis, stratification and prognosis of disorders and conditions, especially cancers.